ACETYLCHOLINESTERASE, I. LARGE-SCALE PURIFICATION, HOMOGENEITY, AND AMINO ACID ANALYSIS
- 1 February 1967
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 57 (2), 446-451
- https://doi.org/10.1073/pnas.57.2.446
Abstract
Purification of ACh [acetylcholine]-esterase of electric tissue of Electrophorus electricus is described. The preparation obtained appears to be a homogeneous protein, as tested by disk electrophoresis and high-speed centrifugation. Starting with 10 kg of toluene-treated material, about 60 mg of homogeneous enzyme protein is obtained. For the 1st time, studies of the protein properties of this biologically important enzyme is possible. An analysis of this macromolecule appears pertinent for the understanding of its function in the elementary processes of excitable membranes during their activity.This publication has 7 references indexed in Scilit:
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